Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Spliced isoforms of the cardiac Nav1.5 channel modify channel activation by distinct structural mechanisms.

The Journal of general physiology - 2 May 2022

Mancino Adamo S, Glass William G, Yan Yuhao, Biggin Philip C, Bowie Derek

Abstract excerpt

Alternative splicing is an important cellular mechanism that fine tunes the gating properties of both voltage- and ligand-gated ion-channels. The cardiac voltage-gated sodium channel, Nav1.5, is subject to alternative splicing of the DI S3-S4 linker, which generates two types of channels with different activation properties. Here, we show that the gating differences between the adult (mH1) and neonatal (Nav1.5e)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Electrophysiological Phenomena
Share to Infant, Newborn

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to NAV1.5 Voltage-Gated Sodium Channel

Share to Protein Isoforms

Share to Voltage-Gated Sodium Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 35297947
DOI: 10.1085/jgp.202112906
PMCID: PMC8939363

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Spliced isoforms of the cardiac Nav1.5 channel modify channel activation by distinct structural mechanisms.PMID 35297947Read ↗

A New Cardiac Channelopathy: From Clinical Phenotypes to Molecular Mechanisms Associated With Nav1.5 Gating PoresSemantic proximity Read ↗

Structural basis of human Nav1.5 gating mechanismsSemantic proximity Read ↗

The cardiac sodium channel: gating function and molecular pharmacology.Semantic proximity Read ↗

Gain-of-function mutation of Nav1.5 in atrial fibrillation enhances cellular excitability and lowers the threshold for action potential firing.Semantic proximity Read ↗

Comparative structural analysis of human Nav1.1 and Nav1.5 reveals mutational hotspots for sodium channelopathies.Semantic proximity Read ↗

Characterization of 2 genetic variants of Na(v) 1.5-arginine 689 found in patients with cardiac arrhythmias.Semantic proximity Read ↗

Biophysical Characterization of A Novel <i>SCN5A</i> Mutation Associated with an Atypical Phenotype of Atrial and Ventricular Arrhythmias and Sudden DeathSemantic proximity Read ↗

The cardiac sodium channel gene SCN5A and its gene product NaV1.5: Role in physiology and pathophysiology.Semantic proximity Read ↗

Inherited cardiac diseases caused by mutations in the Nav1.5 sodium channel.Semantic proximity Read ↗

Molecular bases for the asynchronous activation of sodium and potassium channels required for nerve impulse generation.Semantic proximity Read ↗

Investigating the Functional Role of the DI-DII Linker in Nav1.5 Channel FunctionSemantic proximity Read ↗

Direct Measurement of Cardiac Na+ Channel Conformations Reveals Molecular Pathologies of Inherited Mutations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.